ID   B4GT2_HUMAN             Reviewed;         372 AA.
AC   O60909; B3KTP0; B4DE14; D3DPY6; D3DPY7; O60511; Q4V9L9; Q5T4X5; Q5T4Y5;
AC   Q9BUP6; Q9NSY7;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 193.
DE   RecName: Full=Beta-1,4-galactosyltransferase 2 {ECO:0000305};
DE            Short=Beta-1,4-GalTase 2 {ECO:0000303|PubMed:9405390};
DE            Short=Beta4Gal-T2;
DE            Short=b4Gal-T2 {ECO:0000303|PubMed:9405390};
DE            EC=2.4.1.- {ECO:0000269|PubMed:9405390};
DE   AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE   AltName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase {ECO:0000303|PubMed:9405390};
DE            EC=2.4.1.38 {ECO:0000269|PubMed:9405390};
DE   AltName: Full=Lactose synthase A protein;
DE            EC=2.4.1.22;
DE   AltName: Full=N-acetyllactosamine synthase {ECO:0000303|PubMed:9405390};
DE            EC=2.4.1.90 {ECO:0000269|PubMed:9405390};
DE   AltName: Full=Nal synthase;
DE   AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2;
DE   AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2;
GN   Name=B4GALT2 {ECO:0000312|HGNC:HGNC:925};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=9405390; DOI=10.1074/jbc.272.51.31979;
RA   Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G.,
RA   van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H.;
RT   "A family of human beta4-galactosyltransferases. Cloning and expression of
RT   two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-
RT   galactosyltransferases, beta4Gal-T2 and beta4Gal-T3.";
RL   J. Biol. Chem. 272:31979-31991(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9597550; DOI=10.1093/glycob/8.5.517;
RA   Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.;
RT   "The expanding beta 4-galactosyltransferase gene family: messages from the
RT   databanks.";
RL   Glycobiology 8:517-526(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   CATALYTIC ACTIVITY.
RC   TISSUE=Erythroleukemia;
RX   PubMed=11588157; DOI=10.1093/glycob/11.10.813;
RA   Guo S., Sato T., Shirane K., Furukawa K.;
RT   "Galactosylation of N-linked oligosaccharides by human beta-1,4-
RT   galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells.";
RL   Glycobiology 11:813-820(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-122.
RC   TISSUE=Chondrosarcoma;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-372 (ISOFORMS 1/2).
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   REVIEW.
RX   PubMed=10580128; DOI=10.1016/s0304-4165(99)00168-3;
RA   Amado M., Almeida R., Schwientek T., Clausen H.;
RT   "Identification and characterization of large galactosyltransferase gene
RT   families: galactosyltransferases for all functions.";
RL   Biochim. Biophys. Acta 1473:35-53(1999).
CC   -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC       oligosaccharides in many glycoproteins as well as the carbohydrate
CC       moieties of glycolipids (PubMed:9405390). Can produce lactose
CC       (PubMed:9405390). {ECO:0000269|PubMed:9405390}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP;
CC         Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22;
CC         Evidence={ECO:0000269|PubMed:9405390};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405;
CC         Evidence={ECO:0000269|PubMed:9405390};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC         galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC         derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC         ChEBI:CHEBI:133507; EC=2.4.1.38;
CC         Evidence={ECO:0000269|PubMed:9405390};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC         Evidence={ECO:0000269|PubMed:9405390};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-
CC         galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP;
CC         Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227;
CC         EC=2.4.1.90; Evidence={ECO:0000269|PubMed:11588157,
CC         ECO:0000269|PubMed:9405390};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC         Evidence={ECO:0000269|PubMed:9405390};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=71 uM for GlcNAc-B-S-pNP {ECO:0000269|PubMed:11588157};
CC         KM=0.011 mM for UDP-galactose {ECO:0000269|PubMed:9405390};
CC         KM=0.16 mM for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390};
CC         KM=2.65 mM for D-GlcNAc {ECO:0000269|PubMed:9405390};
CC         Vmax=207.6 pmol/min/mg enzyme towards UDP-galactose
CC         {ECO:0000269|PubMed:9405390};
CC         Vmax=352 pmol/min/mg enzyme towards for benzyl-beta-D-GlcNAc
CC         {ECO:0000269|PubMed:9405390};
CC         Vmax=237.6 pmol/min/mg enzyme towards D-GlcNAc
CC         {ECO:0000269|PubMed:9405390};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- INTERACTION:
CC       O60909-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12261054, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC       pass type II membrane protein. Note=Trans cisternae of Golgi stack.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O60909-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60909-2; Sequence=VSP_014103, VSP_014104;
CC       Name=3;
CC         IsoId=O60909-3; Sequence=VSP_043010;
CC   -!- TISSUE SPECIFICITY: Weakly expressed in various tissues. Highest
CC       expression in prostate, testis, ovary, intestine, muscle, and in fetal
CC       brain. {ECO:0000269|PubMed:9405390}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Beta-1,4-galactosyltransferase 2;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_437";
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DR   EMBL; Y12510; CAA73112.1; -; mRNA.
DR   EMBL; AF038660; AAC39733.1; -; mRNA.
DR   EMBL; AB024434; BAA75819.1; -; mRNA.
DR   EMBL; AK095873; BAG53152.1; -; mRNA.
DR   EMBL; AK293418; BAG56925.1; -; mRNA.
DR   EMBL; AL139220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL357079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07062.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07063.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07064.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07065.1; -; Genomic_DNA.
DR   EMBL; BC096821; AAH96821.1; -; mRNA.
DR   EMBL; AL137647; CAB70857.1; -; mRNA.
DR   CCDS; CCDS506.1; -. [O60909-1]
DR   CCDS; CCDS55596.1; -. [O60909-3]
DR   PIR; T46511; T46511.
DR   RefSeq; NP_001005417.1; NM_001005417.2. [O60909-1]
DR   RefSeq; NP_003771.1; NM_003780.4. [O60909-1]
DR   RefSeq; NP_085076.2; NM_030587.2. [O60909-3]
DR   RefSeq; XP_016858205.1; XM_017002716.1. [O60909-1]
DR   RefSeq; XP_016858206.1; XM_017002717.1. [O60909-1]
DR   AlphaFoldDB; O60909; -.
DR   SMR; O60909; -.
DR   BioGRID; 114247; 142.
DR   IntAct; O60909; 4.
DR   MINT; O60909; -.
DR   STRING; 9606.ENSP00000310696; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GlyCosmos; O60909; 3 sites, No reported glycans.
DR   GlyGen; O60909; 3 sites.
DR   iPTMnet; O60909; -.
DR   PhosphoSitePlus; O60909; -.
DR   SwissPalm; O60909; -.
DR   BioMuta; B4GALT2; -.
DR   jPOST; O60909; -.
DR   MassIVE; O60909; -.
DR   MaxQB; O60909; -.
DR   PaxDb; 9606-ENSP00000310696; -.
DR   PeptideAtlas; O60909; -.
DR   ProteomicsDB; 49666; -. [O60909-1]
DR   ProteomicsDB; 49667; -. [O60909-2]
DR   ProteomicsDB; 49668; -. [O60909-3]
DR   Antibodypedia; 32429; 219 antibodies from 27 providers.
DR   DNASU; 8704; -.
DR   Ensembl; ENST00000309519.8; ENSP00000310696.7; ENSG00000117411.18. [O60909-3]
DR   Ensembl; ENST00000356836.10; ENSP00000349293.6; ENSG00000117411.18. [O60909-1]
DR   Ensembl; ENST00000372324.6; ENSP00000361399.1; ENSG00000117411.18. [O60909-1]
DR   Ensembl; ENST00000434555.7; ENSP00000407468.3; ENSG00000117411.18. [O60909-1]
DR   GeneID; 8704; -.
DR   KEGG; hsa:8704; -.
DR   MANE-Select; ENST00000372324.6; ENSP00000361399.1; NM_003780.5; NP_003771.1.
DR   UCSC; uc001clg.4; human. [O60909-1]
DR   AGR; HGNC:925; -.
DR   CTD; 8704; -.
DR   DisGeNET; 8704; -.
DR   GeneCards; B4GALT2; -.
DR   HGNC; HGNC:925; B4GALT2.
DR   HPA; ENSG00000117411; Low tissue specificity.
DR   MIM; 604013; gene.
DR   neXtProt; NX_O60909; -.
DR   OpenTargets; ENSG00000117411; -.
DR   PharmGKB; PA25224; -.
DR   VEuPathDB; HostDB:ENSG00000117411; -.
DR   eggNOG; KOG3916; Eukaryota.
DR   GeneTree; ENSGT00940000159367; -.
DR   HOGENOM; CLU_044391_0_0_1; -.
DR   InParanoid; O60909; -.
DR   OMA; RPMYTNV; -.
DR   OrthoDB; 306273at2759; -.
DR   PhylomeDB; O60909; -.
DR   TreeFam; TF312834; -.
DR   BioCyc; MetaCyc:HS04130-MONOMER; -.
DR   BRENDA; 2.4.1.38; 2681.
DR   BRENDA; 2.4.1.90; 2681.
DR   PathwayCommons; O60909; -.
DR   Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR   SABIO-RK; O60909; -.
DR   SignaLink; O60909; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 8704; 21 hits in 1164 CRISPR screens.
DR   ChiTaRS; B4GALT2; human.
DR   GeneWiki; B4GALT2; -.
DR   GenomeRNAi; 8704; -.
DR   Pharos; O60909; Tbio.
DR   PRO; PR:O60909; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O60909; Protein.
DR   Bgee; ENSG00000117411; Expressed in cortical plate and 174 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004461; F:lactose synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003945; F:N-acetyllactosamine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR   GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR   CDD; cd00899; b4GalT; 1.
DR   InterPro; IPR003859; Galactosyl_T.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR027995; Galactosyl_T_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF32; BETA-1,4-GALACTOSYLTRANSFERASE 2; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; O60909; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..372
FT                   /note="Beta-1,4-galactosyltransferase 2"
FT                   /id="PRO_0000080533"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..372
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          56..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150..154
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..191
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..218
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         280..283
FT                   /ligand="N-acetyl-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:506227"
FT                   /evidence="ECO:0000250"
FT   BINDING         311..313
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="N-acetyl-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:506227"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        97..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..230
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..118
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_014103"
FT   VAR_SEQ         1
FT                   /note="M -> MAVEVQEQWPCLPAAGCPGPLGGPVAACGM (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043010"
FT   VAR_SEQ         119
FT                   /note="E -> MPSTQLLAAAAAAATAPGPTPPPLAPGSLRSPVPCPVPRLPRCHPVL
FT                   TRHLVL (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_014104"
FT   VARIANT         122
FT                   /note="Q -> H (in dbSNP:rs1859728)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_020487"
FT   VARIANT         338
FT                   /note="G -> R (in dbSNP:rs35904809)"
FT                   /id="VAR_054021"
FT   CONFLICT        100
FT                   /note="S -> TS (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="P -> S (in Ref. 2; AAC39733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="G -> C (in Ref. 2; AAC39733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315..316
FT                   /note="KH -> ND (in Ref. 2; AAC39733)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   372 AA;  41972 MW;  A6F7800251AA1E4F CRC64;
     MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSARGP AHALHPAASS
     SSSSSNCSRP NATASSSGLP EVPSALPGPT APTLPPCPDS PPGLVGRLLI EFTSPMPLER
     VQRENPGVLM GGRYTPPDCT PAQTVAVIIP FRHREHHLRY WLHYLHPILR RQRLRYGVYV
     INQHGEDTFN RAKLLNVGFL EALKEDAAYD CFIFSDVDLV PMDDRNLYRC GDQPRHFAIA
     MDKFGFRLPY AGYFGGVSGL SKAQFLRING FPNEYWGWGG EDDDIFNRIS LTGMKISRPD
     IRIGRYRMIK HDRDKHNEPN PQRFTKIQNT KLTMKRDGIG SVRYQVLEVS RQPLFTNITV
     DIGRPPSWPP RG
//